ArticlePloS one2014
In silico and in vitro studies on the protein-protein interactions between Brugia malayi immunomodulatory protein calreticulin and human C1q.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 47 citations in OpenAlex.
- Localization of the Complement C1q-Binding Site onTropical medicine and infectious disease · 2026Article
- The Interaction BetweenPathogens (Basel, Switzerland) · 2026Article
- Nematodes immunomodulatory mechanisms and possible clinical application.Frontiers in immunology · 2026Review
- A novel calreticulin of Psoroptes ovis regulated keratinocyte function resulting in host skin barrier dysfunction: implications for involvement in the pathogenesis of psoroptic mange.Parasites & vectors · 2025Article
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- In vitro immunoregulatory role of recombinant Ancylostoma ceylanicum calreticulin.Parasites, hosts and diseases · 2024Article
- Crystal structure ofFrontiers in immunology · 2024Article
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- The many faces of parasite calreticulin.Frontiers in immunology · 2023Review
- Harnessing Immune Evasion Strategy of Lymphatic Filariae: A Therapeutic Approach against Inflammatory and Infective Pathology.Vaccines · 2022Review
- Immunoreactivity of Brugia malayi Calreticulin and Its Domains with Sera of Different Categories of Bancroftian Filarial Patients.Acta parasitologica · 2022Article
- Immunoinformatics design of a novel epitope-based vaccine candidate against dengue virus.Scientific reports · 2021Article
- Structure insights of SARS-CoV-2 open state envelope protein and inhibiting through active phytochemical of ayurvedic medicinal plants fromSaudi journal of biological sciences · 2021Article
- IFN-γCellular immunology · 2021Article
- The Secretome of Filarial Nematodes and Its Role in Host-Parasite Interactions and Pathogenicity in Onchocerciasis-Associated Epilepsy.Frontiers in cellular and infection microbiology · 2021Review
- Article
- The Interactions of Parasite Calreticulin With Initial Complement Components: Consequences in Immunity and Virulence.Frontiers in immunology · 2020Review
- Transcriptome-wide analysis of filarial extract-primed human monocytes reveal changes in LPS-induced PTX3 expression levels.Scientific reports · 2019Article
- Complement Evasion: An Effective Strategy That Parasites Utilize to Survive in the Host.Frontiers in microbiology · 2019Review
- Mapping of the complement C1q binding site on Trichinella spiralis paramyosin.Parasites & vectors · 2018Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Filarial parasites modulate effective immune response of their host by releasing a variety of immunomodulatory molecules, which help in the long persistence of the parasite within the host. The present study was aimed to characterize an immunomodulatory protein of Brugia malayi and its interaction with the host immune component at the structural and functional level. Our findings showed that Brugia malayi Calreticulin (BmCRT) is responsible for the prevention of classical complement pathway activation via its interaction with the first component C1q of the human host. This was confirmed by inhibition of C1q dependent lysis of immunoglobulin-sensitized Red Blood Cells (S-RBCs). This is possibly the first report which predicts CRT-C1q interaction on the structural content of proteins to explain how BmCRT inhibits this pathway. The molecular docking of BmCRT-C1q complex indicated that C1qB chain (IgG/M and CRP binding sites on C1q) played a major role in the interaction with conserved and non-conserved regions of N and P domain of BmCRT. Out of 37 amino acids of BmCRT involved in the interaction, nine amino acids (Pro(126), Glu(132), His(147), Arg(151), His(153), Met(154), Lys(156), Ala(196) and Lys(212)) are absent in human CRT. Both ELISA and in silico analysis showed the significant role of Ca(+2) in BmCRT-HuC1q complex formation and deactivation of C1r2-C1s2. Molecular dynamics studies of BmCRT-HuC1q complex showed a deviation from ∼ 0.4 nm to ∼ 1.0 nm. CD analyses indicated that BmCRT is composed of 49.6% α helix, 9.6% β sheet and 43.6% random coil. These findings provided valuable information on the architecture and chemistry of BmCRT-C1q interaction and supported the hypothesis that BmCRT binds with huC1q at their targets (IgG/M, CRP) binding sites. This interaction enables the parasite to interfere with the initial stage of host complement activation, which might be helpful in parasites establishment. These results might be utilized for help in blocking the C1q/CRT interaction and preventing parasite infection.
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